SYA_PROM5
ID SYA_PROM5 Reviewed; 886 AA.
AC A2BTZ9;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Alanine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00036};
DE EC=6.1.1.7 {ECO:0000255|HAMAP-Rule:MF_00036};
DE AltName: Full=Alanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00036};
DE Short=AlaRS {ECO:0000255|HAMAP-Rule:MF_00036};
GN Name=alaS {ECO:0000255|HAMAP-Rule:MF_00036}; OrderedLocusNames=P9515_00511;
OS Prochlorococcus marinus (strain MIT 9515).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167542;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9515;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(2007).
CC -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a two-
CC step reaction: alanine is first activated by ATP to form Ala-AMP and
CC then transferred to the acceptor end of tRNA(Ala). Also edits
CC incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing
CC domain. {ECO:0000255|HAMAP-Rule:MF_00036}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-
CC tRNA(Ala); Xref=Rhea:RHEA:12540, Rhea:RHEA-COMP:9657, Rhea:RHEA-
CC COMP:9923, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78497, ChEBI:CHEBI:456215; EC=6.1.1.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00036};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00036};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00036};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00036}.
CC -!- DOMAIN: Consists of three domains; the N-terminal catalytic domain, the
CC editing domain and the C-terminal C-Ala domain. The editing domain
CC removes incorrectly charged amino acids, while the C-Ala domain, along
CC with tRNA(Ala), serves as a bridge to cooperatively bring together the
CC editing and aminoacylation centers thus stimulating deacylation of
CC misacylated tRNAs. {ECO:0000255|HAMAP-Rule:MF_00036}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00036}.
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DR EMBL; CP000552; ABM71260.1; -; Genomic_DNA.
DR RefSeq; WP_011819377.1; NC_008817.1.
DR AlphaFoldDB; A2BTZ9; -.
DR SMR; A2BTZ9; -.
DR STRING; 167542.P9515_00511; -.
DR EnsemblBacteria; ABM71260; ABM71260; P9515_00511.
DR KEGG; pmc:P9515_00511; -.
DR eggNOG; COG0013; Bacteria.
DR HOGENOM; CLU_004485_1_0_3; -.
DR OMA; YHHTMFE; -.
DR OrthoDB; 91428at2; -.
DR Proteomes; UP000001589; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.930.10; -; 1.
DR HAMAP; MF_00036_B; Ala_tRNA_synth_B; 1.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR002318; Ala-tRNA-lgiase_IIc.
DR InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd.
DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core.
DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N.
DR InterPro; IPR023033; Ala_tRNA_ligase_euk/bac.
DR InterPro; IPR003156; DHHA1_dom.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR012947; tRNA_SAD.
DR Pfam; PF02272; DHHA1; 1.
DR Pfam; PF01411; tRNA-synt_2c; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR00980; TRNASYNTHALA.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF101353; SSF101353; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR SUPFAM; SSF55186; SSF55186; 1.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00344; alaS; 1.
DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; RNA-binding; tRNA-binding; Zinc.
FT CHAIN 1..886
FT /note="Alanine--tRNA ligase"
FT /id="PRO_0000347729"
FT BINDING 564
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 568
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 666
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
FT BINDING 670
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00036"
SQ SEQUENCE 886 AA; 99763 MW; EE03805B6B33EF38 CRC64;
MKSQSQATPI TGDEIRKAFL DFYESKSHLI IPSSSLIPDD PTVMLTIAGM LPFKPVFLGL
RNRPSPRASS SQKCLRTNDI ENVGVTARHH TFFEMLGNFS FGDYFKKEAI QWAWELITDI
YHLKPENIII SVFHEDHESE KIWRDNIGII PERIIRLDEK DNFWSSGATG PCGPCSELYY
DFNPEKGLKN IDLEDGDRFI EFYNLVFMQY NRDSNGMLSD LKFKNIDTGM GLERMAQILQ
KKTNNYETDL ILPIVKEAAL IANIDYFSSD DRTKISLKIL GDHTRAIIHL ISDGVVASNL
GRGYILRRLL RRMIRHGRLL AIKDDFLSRL ASIGISLMQN TYPDLKNNKE RILREINIEE
KRFLETLDRG EKLLNDLIRS GEKLISGTKA FELYDTYGFP LELTKEILEE KNINVDLEGF
TREMEAQKER AKAASQKIDL TLKGSIEREI DLFDQTIFEG YDSLNSQGIV KGIFFESNSV
EKAIQGQTVQ IILDQTSFYG ESGGQVGDTG TISRNDAEID IDKVIRKKNI FLHCGTVRKG
EICRNQLVET RVDKFNRAKA ESNHTATHLL QSALKLIIDK SVSQRGSLVG FNKLRFDFNS
PQPLSKEQIS QVESLVNSWI SENHPIEVKN MDKDDALKAG ALAMFGEKYG DIVRVVDVPG
VSMELCGGTH VQTTSEVGSF KIISEIGISS GIRRIEALSG QLVLDYFKER DETVNKLSDL
LKARPSQLFE RIDSLQTELV NKNKEIQRMK DEIAYFKYSS LSSSAKKIGS FSLIINQIDG
LDGSSLQSAA LDLTSKLGDK SVVILGGIPD TEKKKLLFVV SFGDDLVRRG MHAGKLINEI
SRICSGGGGG KPNFAQAGAK DIDKLNDALE YARKDLWEKL LSYSDK
